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Title: A Mechanistic Analysis of Enzymatic Degradation of Organohalogen Compounds
Authors: KURIHARA, Tatsuo  kyouindb  KAKEN_id  orcid https://orcid.org/0000-0002-7777-1378 (unconfirmed)
Author's alias: 栗原, 達夫
Keywords: L-2-haloacid dehalogenase
DL-2-haloacid dehalogenase
fluoroacetate dehalogenase
2-haloacrylate reductase
2-haloacrylate hydratase
Issue Date: Feb-2011
Publisher: Japan Society for Bioscience, Biotechnology, and Agrochemistry
Journal title: Bioscience, Biotechnology, and Biochemistry
Volume: 75
Issue: 2
Start page: 189
End page: 198
Abstract: Enzymes that catalyze the conversion of organohalogen compounds have been attracting a great deal of attention, partly because of their possible applications in environmental technology and the chemical industry. We have studied the mechanisms of enzymatic degradation of various organic halo acids. In the reaction of L-2-haloacid dehalogenase and fluoroacetate dehalogenase, the carboxylate group of the catalytic aspartate residue nucleophilically attacked the α-carbon atom of the substrates to displace the halogen atom. In the reaction catalyzed by DL-2-haloacid dehalogenase, a water molecule directly attacked the substrate to displace the halogen atom. In the course of studies on the metabolism of 2-chloroacrylate, we discovered two new enzymes. 2-Haloacrylate reductase catalyzed the asymmetric reduction of 2-haloacrylate to produce L-2-haloalkanoic acid in an NADPH-dependent manner. 2-Haloacrylate hydratase catalyzed the hydration of 2-haloacrylate to produce pyruvate. The enzyme is unique in that it catalyzes the non-redox reaction in an FADH2-dependent manner.
Rights: (c) 2011 by Japan Society for Bioscience, Biotechnology, and Agrochemistry.
URL: https://www.jstage.jst.go.jp/article/bbb/75/2/75_100746/_article
URI: http://hdl.handle.net/2433/156503
DOI(Published Version): 10.1271/bbb.100746
Appears in Collections:Journal Articles

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